The S-type lectin from calf heart tissue binds selectively to the carbohydrate chains of laminin.
作者： Qun Zhou , Richard D. Cummings
DOI: 10.1016/0003-9861(90)90408-Q
关键词: Agglutinin 、 Lectin 、 Gel electrophoresis 、 Binding site 、 Biology 、 Glycoprotein 、 Laminin 、 Biochemistry 、 Exoglycosidase 、 Heparin 、 Molecular biology
摘要: Abstract We report that the S-type lectin in calf heart tissue, termed agglutinin (CHA), binds to immobilized mouse laminin ligand blotting and solid-phase radioligand binding assays. When compared with other glycoproteins, radioiodinated CHA preferentially laminin. The is saturable a Kd of 9.2 × 10−7 m competitively inhibited by nonradiolabeled as well similar from porcine tissue. Both lactose N-acetyllactosamine are good inhibitors but not heparin. Exoglycosidase treatments demonstrated dependent on terminal sialyl-, fucosyl-, β- or α-linked galactosyl residues, whereas treatment endo-β-galactosidase significantly decreases binding. Thus, selectively poly-N-acetyllactosamine chains complex-type Asn-linked oligosaccharides
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